RPOB_MYCPN
ID RPOB_MYCPN Reviewed; 1391 AA.
AC P78013;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=MPN_516;
GN ORFNames=MP326;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01321};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR EMBL; U00089; AAB95974.1; -; Genomic_DNA.
DR PIR; S73652; S73652.
DR RefSeq; NP_110204.1; NC_000912.1.
DR RefSeq; WP_010874872.1; NC_000912.1.
DR AlphaFoldDB; P78013; -.
DR SMR; P78013; -.
DR IntAct; P78013; 14.
DR STRING; 272634.MPN_516; -.
DR PRIDE; P78013; -.
DR EnsemblBacteria; AAB95974; AAB95974; MPN_516.
DR KEGG; mpn:MPN_516; -.
DR PATRIC; fig|272634.6.peg.570; -.
DR HOGENOM; CLU_000524_4_1_14; -.
DR OMA; FMTWEGY; -.
DR BioCyc; MPNE272634:G1GJ3-846-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 2.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR02013; rpoB; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1391
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047922"
SQ SEQUENCE 1391 AA; 155622 MW; B2F345AB24F18EAD CRC64;
MSQKPSFFQK KYSPTATRRY YGKIATDFVQ PNLADIQIRS YQTFLDHDLE NLIAAYFPIK
SPNDRYTINF KGLRRTAPER NEAQSRSESK TYEIGIYADL ELIDSATGTI KKPRKSKKNS
ATSSVDGVFL TNLPLITRDG VFIVNGIEKF VIAQITRSPG IYMLTKSQLK LSSSRKRVQE
GYVCEVLPAN GSVMLIYISN KKKIEDAFVQ ILLRDAVREG AKIFPITTLL KAFGMSGKEI
LKVFKNNEFI TRSLEAEVYN AKDFLNNVDP EIKNLLREFR DGKTDLRRKG IASDQKIRSL
VSDYVLLEKE HKALSEAKPN DPKVGQLEAD MDELMDKIIT ERAAKHIVHE LSISLRGLEN
TDECPENSYH ALLCSRFFRQ RRYNLSAAGR YKVSRKLRIT ERIYQKTLAC DLHLKNGELL
LKKGTLLVKE EIDKIKQAAQ NNQIDFVQKI KLTTDGSAVN LSPESLLYES LDVYVNNDNF
DVSVPVVGIH NDNDLNKAIT LSDFIASISY VINIPSAIGK YDDIDHLGNK RVKLINELIS
SRLESGITRM ERFLKEKLTI ADGVNRGQQI NEEGQVIEQA EKKELTIKSL INSKPIQIVI
RDFFNTHQLT QFLDHQNPLS ELSNKRRISA MGPGGISRED PNLDIRDVHY SQYGRICPIE
TPEGMNIGLI MSLASFAKID ENGFLMAPYR KIKNGVITDE VEYLTALRED EHIIAEISSL
VNIDENNKIL DKEIIGRYRS MQGLYDPSKI DYIDVAPHQV VSIGSSLIPF LENDDSARAL
MGTNMQRQAY PLIKPYAPVV GTGQEYKIAR DSGLTMLAPC SGTVKYVDNS KITIESDSGE
QHTLDLIKFE RSNQNTCYNH VPLVEKGQRV TKDEVIADGP AVNKSELSLG QNVLVAFTTW
NGYNYEDAIV ISERLVKDDV LTSLTINEYV AQCLSTKNGD EQITRDIPNV SDANKRYLDE
NGIIMVGAEV KEGDVLVGKV SPKGQVEVSP EEKLFKAIFP ESVQNVRDSS LKLPHGGDGI
VSCVKRFSIA NGNELNDGVI EMIKVYVVQK RKIQIGDKLA GRHGNKGVIS KVVPVADMPH
LEDGTPVDIL LNPLGVPSRM NIGQIFEMHL GYAAHNLAKR MLISACFDDK KAQALSTEIN
QPQYKLDRLI TGLKAQITNR GLKDEQAALA QLNNGDIALV LKEIGMSFDD LHFKVATPIF
QGVNFQDLQD IMDEAGLKPA ETHGKFKLID GRTGLPFEKP ISLGIMYIMK LNHMVDDKIH
ARAVGPYSKI TQQPLGGKSQ NGGQRFGEME VWALEAYGAA YNLQELLTIK SDDVQGRNKA
YAAIVKGAAF PEPGIPESFK LLTKELQGLA LSVSFIYDDN TQQDSNNVSI LQADGEQDDL
FNDFEFDTEG Y
